Literature DB >> 15903964

Picosecond thermometer in the amide I band of myoglobin.

Robert H Austin1, Aihua Xie, Lex van der Meer, Britta Redlich, Per-Anker Lindgård, Hans Frauenfelder, Dan Fu.   

Abstract

The amide I and II bands in myoglobin show a heterogeneous temperature dependence, with bands at 6.17 and 6.43 microm which are more intense at low temperatures. The amide I band temperature dependence is on the long wavelength edge of the band, while the short wavelength side has almost no temperature dependence. We compare concepts of anharmonic solid-state crystal physics and chemical physics for the origins of these bands. We suggest that the long wavelength side is composed of those amino acids which hydrogen bond to the hydration shell of the protein, and that temperature dependent bands can be used to determine the time it takes vibrational energy to flow into the hydration shell. We determine that vibrational energy flow to the hydration shell from the amide I takes approximately 20 ps to occur.

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Year:  2005        PMID: 15903964     DOI: 10.1103/PhysRevLett.94.128101

Source DB:  PubMed          Journal:  Phys Rev Lett        ISSN: 0031-9007            Impact factor:   9.161


  4 in total

1.  Dissociation of β-Sheet Stacking of Amyloid β Fibrils by Irradiation of Intense, Short-Pulsed Mid-infrared Laser.

Authors:  Takayasu Kawasaki; Toyonari Yaji; Toshiaki Ohta; Koichi Tsukiyama; Kazuhiro Nakamura
Journal:  Cell Mol Neurobiol       Date:  2018-02-05       Impact factor: 5.046

2.  Tilting after Dutch windmills: probably no long-lived Davydov solitons in proteins.

Authors:  Robert H Austin; Aihua Xie; Dan Fu; Warren W Warren; Britta Redlich; Lex van der Meer
Journal:  J Biol Phys       Date:  2009-02-11       Impact factor: 1.365

Review 3.  Locating and Navigating Energy Transport Networks in Proteins.

Authors:  Korey M Reid; David M Leitner
Journal:  Methods Mol Biol       Date:  2021

4.  Mid-infrared free-electron laser tuned to the amide I band for converting insoluble amyloid-like protein fibrils into the soluble monomeric form.

Authors:  Takayasu Kawasaki; Jun Fujioka; Takayuki Imai; Kanjiro Torigoe; Koichi Tsukiyama
Journal:  Lasers Med Sci       Date:  2014-04-24       Impact factor: 3.161

  4 in total

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